ID   A0A2K2TWJ2_9CLOT        Unreviewed;       305 AA.
AC   A0A2K2TWJ2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=N-acetylneuraminate lyase {ECO:0000313|EMBL:PNV62465.1};
GN   ORFNames=C0033_07800 {ECO:0000313|EMBL:PNV62465.1};
OS   Clostridium sp. chh4-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=2067550 {ECO:0000313|EMBL:PNV62465.1, ECO:0000313|Proteomes:UP000236356};
RN   [1] {ECO:0000313|Proteomes:UP000236356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=chh4-2 {ECO:0000313|Proteomes:UP000236356};
RA   Huang C.-H.;
RT   "Clostridium sp. nov. strain chh-4-2., isolated from the gut of a healthy
RT   Taiwan adult.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNV62465.1}.
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DR   EMBL; PKUU01000006; PNV62465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K2TWJ2; -.
DR   OrthoDB; 9782828at2; -.
DR   Proteomes; UP000236356; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR   PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236356}.
FT   ACT_SITE        139
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        167
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         209
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   305 AA;  33743 MW;  A2068D7347C841D0 CRC64;
     MRNLEKYKGI FPAFYACYDE NGNVSPERVR ALTEFHIKKG VKGVYVNGSS GECIYQSVED
     RKIVLENVME AAKGRLTVIA HVACNNTKDS VELAKHAQSL KVDAIAAIPP IYFHLPEYAI
     AKYWNDMSAA APETDFVIYN IPQLAGVALT QSLFAEMRKN PNVIGVKNSS MPVQDIQMFK
     AAAGDDYVIF NGPDEQFVSG RVIGAQSGIG GTYGVMPELF LKLNSLIENH EMDEACKLQY
     AINDVIYKMC TCHGNLYAAI KEILRINEGL DIGGVREPLP SLIESDYPIV KEAAAMIEDA
     RKRFC
//